Asset Details
Do you wish to reserve the book?
Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling
Do you wish to request the book?
Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling
2015
Overview
Heterotrimeric G proteins, consisting of Gα, Gβ, and Gγsubunits, are a conserved signal transduction mechanism in eukaryotes. However, G protein subunit numbers in diploid plant genomes are greatly reduced as compared with animals and do not correlate with the diversity of functions and phenotypes in which heterotrimeric G proteins have been implicated. In addition to GPA1, the sole canonical Arabidopsis (Arabidopsis thaliana) Gαsubunit, Arabidopsis has three related proteins: the extra-large GTP-binding proteins XLG1, XLG2, and XLG3. We demonstrate that the XLGs can bind Gβγdimers (AGB1 plus a Gγsubunit: AGG1, AGG2, or AGG3) with differing specificity in yeast (Saccharomyces cerevisiae) three-hybrid assays. Our in silico structural analysis shows that XLG3 aligns closely to the crystal structure of GPA1, and XLG3 also competes with GPA1 for Gβγbinding in yeast. We observed interaction of the XLGs with all three Gβγdimers at the plasma membrane in planta by bimolecular fluorescence complementation. Bioinformatic and localization studies identified and confirmed nuclear localization signals in XLG2 and XLG3 and a nuclear export signal in XLG3, which may facilitate intracellular shuttling. We found that tunicamycin, salt, and glucose hypersensitivity and increased stomatal density are agb1-specific phenotypes that are not observed ingpa1mutants but are recapitulated inxlgmutants. Thus, XLG-Gβγheterotrimers provide additional signaling modalities for tuning plant G protein responses and increase the repertoire of G protein heterotrimer combinations from three to 12. The potential for signal partitioning and competition between the XLGs and GPA1 is a new paradigm for plant-specific cell signaling.
Publisher
American Society of Plant Biologists
Subject
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - metabolism
/ Biology
/ Dimers
/ diploidy
/ genome
/ glucose
/ GTP-Binding Proteins - metabolism
/ Heterotrimeric GTP-Binding Proteins - chemistry
/ Heterotrimeric GTP-Binding Proteins - metabolism
/ Nuclear Localization Signals - chemistry
/ Plants
/ Protein Binding - drug effects
/ Protein Subunits - metabolism
/ Proteins
/ Signal Transduction - drug effects
/ Subcellular Fractions - metabolism
/ Two-Hybrid System Techniques
/ Yeasts
